Physical chemistry of polyglutamine: intriguing tales of a monotonous sequence.
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Physicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs)Intrabodies as neuroprotective therapeuticsStructural Mechanisms of Mutant Huntingtin Aggregation Suppression by the Synthetic Chaperonin-like CCT5 Complex Explained by Cryoelectron Tomography.Interaction of the molecular chaperone DNAJB6 with growing amyloid-beta 42 (Aβ42) aggregates leads to sub-stoichiometric inhibition of amyloid formationScalable production in human cells and biochemical characterization of full-length normal and mutant huntingtinStructure prediction of polyglutamine disease proteins: comparison of methods.Glutamine and Asparagine Side Chain Hyperconjugation-Induced Structurally Sensitive Vibrations.Biophysical insights into how surfaces, including lipid membranes, modulate protein aggregation related to neurodegeneration.Trinucleotide repeats: a structural perspectiveProtein misfolding specifies recruitment to cytoplasmic inclusion bodiesFree-Energy Landscape of the Amino-Terminal Fragment of Huntingtin in Aqueous SolutionStable polyglutamine dimers can contain β-hairpins with interdigitated side chains-but not α-helices, β-nanotubes, β-pseudohelices, or steric zippers.C-terminal domain swapping of SSB changes the size of the ssDNA binding siteA coarse-grained model for polyglutamine aggregation modulated by amphipathic flanking sequencesBiochemical characterization of mutants in chaperonin proteins CCT4 and CCT5 associated with hereditary sensory neuropathy.Molecular interaction between the chaperone Hsc70 and the N-terminal flank of huntingtin exon 1 modulates aggregationProbing the Huntingtin 1-17 membrane anchor on a phospholipid bilayer by using all-atom simulationsPolyglutamine- and temperature-dependent conformational rigidity in mutant huntingtin revealed by immunoassays and circular dichroism spectroscopyFolding Landscape of Mutant Huntingtin Exon1: Diffusible Multimers, Oligomers and Fibrils, and No Detectable Monomer.An Analysis of Biomolecular Force Fields for Simulations of Polyglutamine in SolutionIts preferential interactions with biopolymers account for diverse observed effects of trehaloseRestoration of female fertility in Trichoderma reesei QM6a provides the basis for inbreeding in this industrial cellulase producing fungusKinetically competing huntingtin aggregation pathways control amyloid polymorphism and propertiesMultivalent IDP assemblies: Unique properties of LC8-associated, IDP duplex scaffoldsThe emerging role of the first 17 amino acids of huntingtin in Huntington's diseaseEnhanced molecular mobility of ordinarily structured regions drives polyglutamine diseaseCAMELOT: A machine learning approach for coarse-grained simulations of aggregation of block-copolymeric protein sequences.A solenoid design for assessing determinants of parallel β-sheet registration.Differential recruitment efficacy of patient-derived amyloidogenic and myeloma light chain proteins by synthetic fibrils-A metric for predicting amyloid propensity.Identification of novel polyglutamine-expanded aggregation species in spinal and bulbar muscular atrophyConformational properties of polyglutamine sequences in guanidine hydrochloride solutionsMolecular dynamics analysis of the aggregation propensity of polyglutamine segmentsDesign and Optimization of Anti-amyloid Domain Antibodies Specific for β-Amyloid and Islet Amyloid PolypeptideYeast Nab3 protein contains a self-assembly domain found in human heterogeneous nuclear ribonucleoprotein-C (hnRNP-C) that is necessary for transcription termination.Solid-State Nuclear Magnetic Resonance on the Static and Dynamic Domains of Huntingtin Exon-1 Fibrils.Studying polyglutamine aggregation in Caenorhabditis elegans using an analytical ultracentrifuge equipped with fluorescence detection.Aggregation formation in the polyglutamine diseases: protection at a cost?A platform to view huntingtin exon 1 aggregation flux in the cell reveals divergent influences from chaperones hsp40 and hsp70.DNAJB6 is a peptide-binding chaperone which can suppress amyloid fibrillation of polyglutamine peptides at substoichiometric molar ratios.The role of amyloidogenic protein oligomerization in neurodegenerative disease.
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Physical chemistry of polyglutamine: intriguing tales of a monotonous sequence.
description
article científic
@ca
article scientifique
@fr
articol științific
@ro
articolo scientifico
@it
artigo científico
@gl
artigo científico
@pt
artigo científico
@pt-br
artikel ilmiah
@id
artikull shkencor
@sq
artículo científico
@es
name
Physical chemistry of polyglutamine: intriguing tales of a monotonous sequence.
@en
Physical chemistry of polyglutamine: intriguing tales of a monotonous sequence.
@nl
type
label
Physical chemistry of polyglutamine: intriguing tales of a monotonous sequence.
@en
Physical chemistry of polyglutamine: intriguing tales of a monotonous sequence.
@nl
prefLabel
Physical chemistry of polyglutamine: intriguing tales of a monotonous sequence.
@en
Physical chemistry of polyglutamine: intriguing tales of a monotonous sequence.
@nl
P2860
P1476
Physical chemistry of polyglutamine: intriguing tales of a monotonous sequence.
@en
P2093
Ronald Wetzel
P2860
P304
P356
10.1016/J.JMB.2012.01.030
P407
P577
2012-01-27T00:00:00Z